17β-Hydroxysteroid dehydrogenase
class of enzymes

17β-Hydroxysteroid dehydrogenases (17β-HSD, HSD17B) (EC 1.1.1.51), also 17-ketosteroid reductases (17-KSR), are a group of alcohol oxidoreductases which catalyze the reduction of 17-ketosteroids and the dehydrogenation of 17β-hydroxysteroids in steroidogenesis and steroid metabolism. This includes interconversion of DHEA and androstenediol, androstenedione and testosterone, and estrone and estradiol.
The major reactions catalyzed by 17β-HSD (such as the conversion of androstenedione to testosterone) are hydrogenation (reduction) reactions, rather than dehydrogenation (oxidation) reactions.
Reactions
17β-HSDs catalyze the following redox reactions of sex steroids:
20α-Hydroxyprogesterone ↔ Progesterone
DHEATooltip Dehydroepiandrosterone ↔ Androstenediol
Androstenedione ↔ Testosterone
Dihydrotestosterone ↔ 5α-Androstanedione / 3α-Androstanediol / 3β-Androstanediol
Estrone ↔ Estradiol
16α-Hydroxyestrone ↔ Estriol
Activity distribution
Genes
Genes coding for 17β-HSD include:
HSD17B1: Referred to as "estrogenic". Major subtype for activation of estrogens from weaker forms (estrone to estradiol and 16α-hydroxyestrone to estriol). Catalyzes the final step in the biosynthesis of estrogens. Highly selective for estrogens; 100-fold higher affinity for estranes over androstanes. However, also catalyzes the conversion of DHEA into androstenediol. Recently, has been found to inactivate DHT into 3α- and 3β-androstanediol. Expressed primarily in the ovaries and placenta but also at lower levels in the breast epithelium.
The public source identifies “17β-Hydroxysteroid dehydrogenase” as class of enzymes. This brief keeps that definition visible, then builds a research path around 17β-Hydroxysteroid, dehydrogenase and class.
Why this record matters
A short description can identify a subject without explaining its stakes. For “17β-Hydroxysteroid dehydrogenase”, the useful work is to connect “class of enzymes” to the records capable of establishing context and consequence.
The citation trail is more important than the brevity of the summary: it shows where individual claims can be examined in context. The source revision retrieved here is dated Mar 9, 2026. The linked authority identifier is Q86201640. None of the 0 selected statements returned an explicit reference.
A concise general-reference account can conceal disagreements about scope, terminology or the weight assigned to individual sources. The source lead contains qualifying language; that uncertainty should survive quotation, summary and reuse. Authority statements aid reconciliation but still require their own references, qualifiers and ranks to be checked.
How to read it
Use the entry as an orientation point, then follow its citations and revision history. Names, dates and institutional relationships should be checked against the original record.
- Subject orientation
- Search vocabulary
- Locating named sources
The closest primary source, responsible institution and strongest cited specialist reference.
Three-step research path
- Establish the record: confirm the title “17β-Hydroxysteroid dehydrogenase”, its source revision and the description used here.
- Expand the search: follow 17β-Hydroxysteroid dehydrogenase primary sources, 17β-Hydroxysteroid dehydrogenase archive and 17β-Hydroxysteroid research across catalogues and specialist indexes.
- Test the account: compare the strongest cited source with the responsible institution’s current record and note any disagreement.
Questions for further research
- Which source most directly establishes the central claim about “17β-Hydroxysteroid dehydrogenase”?
- What terminology or title could unlock a more precise catalogue search?
- Which institution is responsible for the underlying evidence?
Search terms from this dossier
This entry incorporates text from “17β-Hydroxysteroid dehydrogenase” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.